Peroxycarboxylic acids (“peracids”) are effective antimicrobial agents. Methods to clean, disinfect, and/or sanitize hard surfaces, food products, living plant tissues, and medical devices against undesirable microbial growth have been described (e.g., U.S. Pat. No. 6,545,047; U.S. Pat. No. 6,183,807; U.S. Pat. No. 6,518,307; U.S. Pat. No. 5,683,724; and U.S. Pat. No. 6,635,286). Peracids have also been reported to be useful in preparing bleaching compositions for laundry detergent applications (e.g., U.S. Pat. No. 3,974,082; U.S. Pat. No. 5,296,161; and U.S. Pat. No. 5,364,554).
Perhydrolytic enzymes may be used to produce peracids. U.S. Patent Application Publication Nos. 2008-0176783 A1; 2008-0176299 A1; 2009-0005590 A1; and 2010-0041752 A1 to DiCosimo et al. disclose enzymes structurally classified as members of the CE-7 family of carbohydrate esterases (i.e., cephalosporin C deacetylases [CAHs] and acetyl xylan esterases [AXEs]) that are characterized by significant perhydrolytic activity for converting carboxylic acid ester substrates (in the presence of a suitable source of peroxygen, such as hydrogen peroxide) into peracids at concentrations sufficient for use as a disinfectant and/or a bleaching agent. Some members of the CE-7 family of carbohydrate esterases have been demonstrated to have perhydrolytic activity sufficient to produce 4000-5000 ppm peracetic acid from acetyl esters of alcohols, diols, and glycerols in 1 minute and up to 9000 ppm between 5 minutes and 30 minutes once the reaction components were mixed (DiCosimo et al., U.S. 2009-0005590 A1). U.S. Patent Application Publication No. 2010-0087529 A1 describes variant CE-7 enzymes having improved perhydrolytic activity.
Peracids are powerful oxidizing agents capable of reaction with a variety of materials. As such, care should be taken when using peracids in applications where the oxidation of non-targeted materials may be undesirable. Certain peracid applications may benefit from a controlled delivery to a target surface to help minimize unwanted oxidation of non-targeted materials.
One way to control delivery of a peracid to a target surface is to target/localize production of the peracid on or near the target surface. Targeted peracid production may decrease the amount of unwanted oxidation of non-targeted materials and may reduce the amount of peracid (or peracid generating components, including perhydrolase) required to achieve the desired effect (such as bleaching, destaining, deodorizing, sanitizing, disinfecting, and cleaning).
Peptidic affinity materials having affinity for a target surface (large peptidic materials such as antibodies, antibody fragments (Fab), single chain fused variable region antibodies (scFc), Camelidae antibodies, and scaffold display proteins) have been used to direct benefit agents to a target surface. Typically the benefit agent is coupled directly to the peptidic material having affinity for the target surface. However, the cost and complexity of using these large peptidic affinity materials may exclude them for use in certain applications.
The use of shorter peptides having strong affinity for a target surface to target a benefit agent to a target surface has been described (U.S. Pat. Nos. 7,220,405; 7,309,482; 7,285,264 and 7,807,141; U.S. Patent Application Publication Nos. 2005-0226839 A1; 2007-0196305 A1; 2006-0199206 A1; 2007-0065387 A1; 2008-0107614 A1; 2007-0110686 A1; 2006-0073111 A1; 2010-0158846; and 2010-0158847; and published PCT applications WO2008/054746; WO2004/048399, and WO2008/073368). However, the use of such a peptidic material having affinity for a target surface to couple a perhydrolytic enzyme catalyst (i.e., “targeted perhydrolases”) to the surface for the production of a peracid benefit agent has not been described.
Some target surfaces that may benefit from a peracid treatment may be comprised of a cellulosic material. As such, materials having affinity for cellulosic materials may be useful for targeted peracid treatment. Cellulose-binding domains (CBDs) have been identified in a large number of proteins typically associated with cellulose degradation. Tomme et al. (J. Chromatogr. B (1998) 7125: 283-296) discloses 13 families of cellulose-binding domains and their use in affinity purification applications. EP1224270B1 discloses synthetic “mimic” cellulose-binding domains that are typically no more than 30 amino acids in length and have strong affinity for cellulosic substances. WO2005/042735 A1 discloses non-catalytic carbohydrate-binding molecules from glucosyl hydrolase family 61 having affinity for cellulose. Han et al. (Shengwu Huaxue Yu Shengwu Wuli Xuebao 30:263 266 (1998)) describes the identification of peptides that specifically bind to a cellulose matrix using the phage display method. The deduced amino acid sequences of these cellulose-binding peptides have a conserved aromatic residue, tyrosine or phenylalanine, which is similar to the normal cellulose binding domain of some cellulose-binding proteins.
The use of cellulose-binding domains in the creation of fusion proteins and chimeric peptidic constructs for the targeted delivery of a benefit agent in laundry care applications has been reported. U.S. Pat. No. 7,361,487 discloses cellulase fusion proteins comprising an endoglucanase core coupled to a heterologous cellulose binding domain for use in denim finishing. CN101591648A discloses a fusion protein comprising a cutinase fused to a cellulose binding domain for cotton fiber finishing. U.S. Patent Application Publication 2006-0246566 discloses cellulase fusion proteins comprising a neutral cellulase core of a Melanocarpus sp. and a tail consisting of a linker/cellulose binding domain of an acid cellobiohydrolase I of Trichoderma reesei. 
WO97/40229 and WO97/40127 disclose a method of treating fabrics with a cellulase and a hybrid enzyme comprising a phenol oxidizing enzyme fused a cellulose binding domain. U.S. Pat. No. 6,017,751 discloses a fusion protein comprising a cellulose-binding domain fused to an α-amylase, a lipase, a peroxidase or a laccase.
U.S. Pat. No. 6,586,384 and U.S. Pat. No. 6,579,842 disclose methods of delivering a benefit agent to a selected area of fabric for exerting a predetermined activity using a multi-specific binding molecule that is pre-treated on the fabric followed by contacting the pre-treated fabric with the benefit agent. The binding molecule may be a fusion protein comprising a cellulose-binding domain fused to a second portion having affinity for the benefit agent.
U.S. Pat. No. 6,919,428 discloses a fusion protein comprising a cellulose-binding domain and a protein having affinity for another ligand and detergent compositions comprising such fusion proteins. U.S. Pat. No. 7,041,793 discloses detergent compositions comprising a fusion protein having a cellulose-binding domain coupled to an antibody or antibody fragment which has affinity for another ligand. U.S. Pat. No. 6,410,498 discloses laundry detergent and fabric care compositions comprising a modified transferase comprising a cellulose-binding domain. WO99/57250 discloses modified enzymes comprising a catalytically active amino acid sequence linked via a non-amino acid linker to a region comprising a cellulose-binding domain.
U.S. Pat. No. 6,465,410 discloses laundry detergents and fabric care compositions comprising modified proteins having a catalytically active amino acid sequence of an antimicrobial peptide or protein linked to an amino acid sequence comprising a cellulose-binding domain for improved sanitization benefits. U.S. Pat. No. 6,906,024 discloses fabric care compositions comprising a fabric softening peptide coupled via a non-amino acid linker to one of four specific cellulose binding domains.
WO2000/018865 and EP1115828B1 disclose a chemical entity comprising a cellulose-binding domain coupled to a chemical component for use in laundry care applications. WO2005/051997 discloses a fusion protein comprising a cellulose-binding domain from a fungal enzyme and a domain having affinity for a melamine-type polymer used to encapsulate a benefit agent.
Some woven and non-woven materials may be comprised of synthetic materials such as polyamides, nylons, polyurethanes, polyacrylates, polyesters, polyolefins, polylactides, and semi-synthetic materials such as cellulose acetate. As such, peptide-binding domains having affinity for any of these and other synthetic or semi-synthetic materials used in the manufacture of textiles may also aid in the targeted delivery of a perhydrolytic enzyme.
Biopanned peptides having affinity for cellulose and non-cellulosic materials such as cotton fabrics, polyester/cotton blends, cellulose acetate, paper, polymethyl methacrylate, Nylon, polypropylene, polyethylene, polystyrene, and polytetrafluoroethylene have been reported (U.S. Pat. Nos. 7,709,601; 7,700,716; 7,632,919; 7,858,581; 7,928,076; and 7,906,617; and U.S. Patent Application Publication NOs. 2005-0054752; 2010-0310495; 2010-0298231; 2010-0298240; 2010-0298241; 2010-0298531; 2010-0298532; 2010-0298533; 2010-0298534; and 2010-0298535. The use of such peptides in fusion proteins for targeted peracid production has not been described.
WO 01/79479 to Estell et al. discloses a modified phage display screening method that comprises contacting a peptide library with an anti-target to remove peptides that bind to the anti-target, then contacting the non-binding peptides with the target. Using this method, peptide sequences that bind to collar soil, but not to polyester/cotton and peptide sequences that bind to polyurethane, but not to cotton, polyester, or polyester/cotton fabrics were identified. No peptide sequences that bind to fabrics are reported in that disclosure.
The problem to be solved it to provide compositions and methods to target enzymatic peracid production to the surface of a target material to provide a peracid-based benefit to the target surface.